scholarly journals The role of rendering in relation to the bovine spongiform encephalopathy epidemic, the development of EU animal by‐product legislation and the reintroduction of rendered products into animal feeds

2021 ◽  
Author(s):  
S. L. Woodgate ◽  
R. G. Wilkinson
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Spongiform Encephalopathy ◽  
Animal Feeds

scholarly journals Prion Protein Devoid of the Octapeptide Repeat Region Delays Bovine Spongiform Encephalopathy Pathogenesis in Mice

2017 ◽  
Vol 92 (1) ◽  
Author(s):  
Hideyuki Hara ◽  
Hironori Miyata ◽  
Nandita Rani Das ◽  
Junji Chida ◽  
Tatenobu Yoshimochi ◽  
...  
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Prion Protein ◽  
Prion Diseases ◽  
Spongiform Encephalopathy ◽  
Wild Type ◽  
Jakob Disease ◽  
Function Relationship ◽  
Different Strains ◽  
Conformational Conversion

ABSTRACTConformational conversion of the cellular isoform of prion protein, PrPC, into the abnormally folded, amyloidogenic isoform, PrPSc, is a key pathogenic event in prion diseases, including Creutzfeldt-Jakob disease in humans and scrapie and bovine spongiform encephalopathy (BSE) in animals. We previously reported that the octapeptide repeat (OR) region could be dispensable for converting PrPCinto PrPScafter infection with RML prions. We demonstrated that mice transgenically expressing mouse PrP with deletion of the OR region on the PrP knockout background, designated Tg(PrPΔOR)/Prnp0/0mice, did not show reduced susceptibility to RML scrapie prions, with abundant accumulation of PrPScΔOR in their brains. We show here that Tg(PrPΔOR)/Prnp0/0mice were highly resistant to BSE prions, developing the disease with markedly elongated incubation times after infection with BSE prions. The conversion of PrPΔOR into PrPScΔOR was markedly delayed in their brains. These results suggest that the OR region may have a crucial role in the conversion of PrPCinto PrPScafter infection with BSE prions. However, Tg(PrPΔOR)/Prnp0/0mice remained susceptible to RML and 22L scrapie prions, developing the disease without elongated incubation times after infection with RML and 22L prions. PrPScΔOR accumulated only slightly less in the brains of RML- or 22L-infected Tg(PrPΔOR)/Prnp0/0mice than PrPScin control wild-type mice. Taken together, these results indicate that the OR region of PrPCcould play a differential role in the pathogenesis of BSE prions and RML or 22L scrapie prions.IMPORTANCEStructure-function relationship studies of PrPCconformational conversion into PrPScare worthwhile to understand the mechanism of the conversion of PrPCinto PrPSc. We show here that, by inoculating Tg(PrPΔOR)/Prnp0/0mice with the three different strains of RML, 22L, and BSE prions, the OR region could play a differential role in the conversion of PrPCinto PrPScafter infection with RML or 22L scrapie prions and BSE prions. PrPΔOR was efficiently converted into PrPScΔOR after infection with RML and 22L prions. However, the conversion of PrPΔOR into PrPScΔOR was markedly delayed after infection with BSE prions. Further investigation into the role of the OR region in the conversion of PrPCinto PrPScafter infection with BSE prions might be helpful for understanding the pathogenesis of BSE prions.

Detection and identification of animal-derived protein in feedingstuffs by enzyme-linked immunoassay

1991 ◽  
Vol 1991 ◽  
pp. 117-117
Author(s):  
P. A. Brett ◽  
P. R. Goodwin
Keyword(s):  
Great Britain ◽  
Bovine Spongiform Encephalopathy ◽  
Animal Species ◽  
Animal Protein ◽  
Spongiform Encephalopathy ◽  
Meat And Bone Meal ◽  
Bone Meal ◽  
Animal Feeds ◽  
Regulatory Authorities ◽  
Detection And Identification

In Great Britain the use of animal-derived protein in animal feeds has recently been subject to restrictions (The Bovine Spongiform Encephalopathy Order 1988 and subsequent orders), including a prohibition on the use of animal protein produced from ruminant carcases in feed given to ruminants. More generally, livestock producers are increasingly demanding more detailed information about the ingredients included in the compound feeds they purchase, and may stipulate that meat and bone meal derived from particular animal species is not used in their feed. In order that compliance with these legal and commercial requirements can be monitored and enforced, it is important that feed manufacturers, their customers and the regulatory authorities should have recourse to a means of identifying the species from which animal protein, when present in a feed, is derived.

Production of prion gene knockout cow to prevent spontaneous bovine spongiform encephalopathy

2014 ◽  
Author(s):  
Noboru Manabe ◽  
Ichiro Onoyama ◽  
Junyou Li ◽  
Yutaka Sendai ◽  
Yoshito Aoyagi
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Gene Knockout ◽  
Spongiform Encephalopathy ◽  
Prion Gene

Abnormalities of heart rate and rhythm in bovine spongiform encephalopathy

1997 ◽  
Vol 141 (14) ◽  
pp. 352-357 ◽  
Author(s):  
A. R. Austin ◽  
L. Pawson ◽  
S. Meek ◽  
S. Webster
Keyword(s):  
Heart Rate ◽  
Bovine Spongiform Encephalopathy ◽  
Spongiform Encephalopathy

scholarly journals Exploration of genetic factors resulting in abnormal disease in cattle experimentally challenged with bovine spongiform encephalopathy

Prion ◽  
2021 ◽  
Vol 15 (1) ◽  
pp. 1-11
Author(s):  
Sandor Dudas ◽  
Renee Anderson ◽  
Antanas Staskevicus ◽  
Gordon Mitchell ◽  
James C. Cross ◽  
...  
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Genetic Factors ◽  
Spongiform Encephalopathy

scholarly journals A Case of Bovine Spongiform Encephalopathy in Denmark

1993 ◽  
Vol 34 (1) ◽  
pp. 99-100
Author(s):  
J. S. Agerholm ◽  
H. V. Krogh ◽  
T. K. Nielsen ◽  
S. Ammendrup ◽  
H. Dalsgaard
Keyword(s):  
Bovine Spongiform Encephalopathy ◽  
Spongiform Encephalopathy
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